6MFK

Crystal Structure of Chloramphenicol Acetyltransferase from Elizabethkingia anophelis

6MFK の概要

• エントリーDOI: 10.2210/pdb6mfk/pdb
• 分子名称: Chloramphenicol acetyltransferase, (4S)-2-METHYL-2,4-PENTANEDIOL, PHOSPHATE ION, ... (4 entities in total)
• 機能のキーワード: ssgcid, transferase, antibiotic resistance, structural genomics, seattle structural genomics center for infectious disease
• 由来する生物種: Elizabethkingia anophelis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 24973.94

構造登録者

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (登録日: 2018-09-11, 公開日: 2018-10-03, 最終更新日: 2023-10-11)

主引用文献

Ghafoori, S.M.,Robles, A.M.,Arada, A.M.,Shirmast, P.,Dranow, D.M.,Mayclin, S.J.,Lorimer, D.D.,Myler, P.J.,Edwards, T.E.,Kuhn, M.L.,Forwood, J.K.
Structural characterization of a Type B chloramphenicol acetyltransferase from the emerging pathogen Elizabethkingia anophelis NUHP1.
Sci Rep, 11:9453-9453, 2021

PubMed Abstract: Elizabethkingia anophelis is an emerging multidrug resistant pathogen that has caused several global outbreaks. E. anophelis belongs to the large family of Flavobacteriaceae, which contains many bacteria that are plant, bird, fish, and human pathogens. Several antibiotic resistance genes are found within the E. anophelis genome, including a chloramphenicol acetyltransferase (CAT). CATs play important roles in antibiotic resistance and can be transferred in genetic mobile elements. They catalyse the acetylation of the antibiotic chloramphenicol, thereby reducing its effectiveness as a viable drug for therapy. Here, we determined the high-resolution crystal structure of a CAT protein from the E. anophelis NUHP1 strain that caused a Singaporean outbreak. Its structure does not resemble that of the classical Type A CATs but rather exhibits significant similarity to other previously characterized Type B (CatB) proteins from Pseudomonas aeruginosa, Vibrio cholerae and Vibrio vulnificus, which adopt a hexapeptide repeat fold. Moreover, the CAT protein from E. anophelis displayed high sequence similarity to other clinically validated chloramphenicol resistance genes, indicating it may also play a role in resistance to this antibiotic. Our work expands the very limited structural and functional coverage of proteins from Flavobacteriaceae pathogens which are becoming increasingly more problematic.

PubMed: 33947893
DOI: 10.1038/s41598-021-88672-z

実験手法

X-RAY DIFFRACTION (1.65 Å)